ID A0A2S0N3T4_9BURK Unreviewed; 715 AA.
AC A0A2S0N3T4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN ORFNames=C6571_17260 {ECO:0000313|EMBL:AVO42814.1};
OS Simplicispira suum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Simplicispira.
OX NCBI_TaxID=2109915 {ECO:0000313|EMBL:AVO42814.1, ECO:0000313|Proteomes:UP000239326};
RN [1] {ECO:0000313|EMBL:AVO42814.1, ECO:0000313|Proteomes:UP000239326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC1-8 {ECO:0000313|EMBL:AVO42814.1,
RC ECO:0000313|Proteomes:UP000239326};
RA Kim S.-J., Heo J., Kwon S.-W.;
RT "Genome sequencing of Simplicispira sp.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC Evidence={ECO:0000256|ARBA:ARBA00023693};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000256|RuleBase:RU003707}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC hydratase/isomerase family. {ECO:0000256|ARBA:ARBA00008750}.
CC -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}.
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DR EMBL; CP027669; AVO42814.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0N3T4; -.
DR KEGG; simp:C6571_17260; -.
DR OrthoDB; 5287258at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000239326; Chromosome.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR CDD; cd06558; crotonase-like; 1.
DR Gene3D; 1.10.1040.50; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR InterPro; IPR006108; 3HC_DH_C.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43612:SF3; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 3: Inferred from homology;
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027}.
FT DOMAIN 317..495
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 498..598
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 715 AA; 77075 MW; FB53EC60EDC9DFB5 CRC64;
MTQNKFLTFE VDAAGIGLAT LDQPGRAMNV LTPVLMEAVA ALVERLEKED SLKGLVLTSG
KPSFIVGADI DQLNQITTID QAFRLGEELK ALMRRMEKCG KPVVAALNGT TLGGGLELAM
ACHARFAMDD PKAKIGLPEV KLGLLPGGGG TQRLPRLIGI QKSLELMTQG TELSPAKALG
LGLLTGLATT REELLQKARD WCLANPKPVQ PWDTKGFRIP GGDSKSPAVV QVLSIAPSMA
NAKAHGNYPA ITHIMSCLFE GCLLDIDNAL QVESRYFAAC IVSQVSKNMI GTLWYQLNAI
KKGQSRPKDV PAGKVKKLGI LGAGMMGAGI AYVSAKVGID VVLLDATQEN AEKGKAYSQG
LLDKALSRSK TTQEKRDALL ARILATTRYE DLQGCDLVIE AVFEDRAIKA ECTRKAEAVI
AADAVFASNT STLPITGLAQ VSSRPANFLG LHFFSPVDKM PLVEIIVGEK TSEETLARGF
DYVLQIGKTP IVVNDSRGFY TSRVFATYVM EGLAMLAEGV HPRSIEVAGI KAGMPMPPLA
LQDEVSLGLS LHVSDQTRRD LETEGKTYPA HPGEAVLRKV GGELGRLGKK AGKGFYDYEG
KEKSLWPELT TLYPPRAEQP TQEELVDRLM FIQANEAARC FEERVVRSVA DTNIGSIFGW
GFAPHQGGAL QFINAMGAQR FVDRSRELAK LHGARFEPAA VVVKMAQEGA RFEDA
//
